ID Q8D2T6_WIGBR Unreviewed; 405 AA.
AC Q8D2T6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=b2817 {ECO:0000313|EMBL:BAC24414.1};
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870 {ECO:0000313|EMBL:BAC24414.1, ECO:0000313|Proteomes:UP000000562};
RN [1] {ECO:0000313|EMBL:BAC24414.1, ECO:0000313|Proteomes:UP000000562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00001561};
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DR EMBL; BA000021; BAC24414.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8D2T6; -.
DR STRING; 36870.gene:10368761; -.
DR KEGG; wbr:b2817; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_1991752_0_0_6; -.
DR Proteomes; UP000000562; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000562};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..393
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT COILED 147..174
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 405 AA; 47726 MW; 112F93C35645F104 CRC64;
MIKIKNIFYL KIVFIYFFLI INYSCSSNIK NINDIFIENE KYTSKINFIS NEKINYNYFI
LYDPYRLIVD FKKTNINLDI KNVNKKIKLN SNTIKLIRLG YFKKNITRLV IELKNYSFFD
IFYLKKNLFS LSIVIYKDKY ISNDYIKKNI SKLINNINEK NKKKENKKKL SKNKSIITIM
LDPGHGGEDP GAIGQKNTYE KNVVLQIAKR IYNLIQKKPY MRVYMTRNKD VFVSLKDRII
KARRKKIDIF ISIHTDSAKK KFVKGASVFS ISRKEANIVA EKYYSNNYHF IENIIGIKKS
NDEYIDHTIF DLIQNFSINE SVKFGKQILN SLEKITDLHK KNIGQAGFAV LKAPEIPSIL
IEIAFISNLQ EEKNLNNSIY QQKVAKAIFE GIEKYYLLNK KKYNH
//
